ID D6A5Z2_STRV1 Unreviewed; 714 AA.
AC D6A5Z2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Acyl-CoA synthetase {ECO:0000313|EMBL:EFE65943.2};
GN ORFNames=SSFG_01196 {ECO:0000313|EMBL:EFE65943.2};
OS Streptomyces viridosporus (strain ATCC 14672 / DSM 40746 / JCM 4963 / KCTC
OS 9882 / NRRL B-12104 / FH 1290) (Streptomyces ghanaensis).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=566461 {ECO:0000313|EMBL:EFE65943.2, ECO:0000313|Proteomes:UP000003824};
RN [1] {ECO:0000313|Proteomes:UP000003824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14672 / DSM 40746 / JCM 4963 / KCTC 9882 / NRRL B-12104 /
RC FH 1290 {ECO:0000313|Proteomes:UP000003824};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M.,
RA Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M.,
RA Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces ghanaensis ATCC 14672.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DS999641; EFE65943.2; -; Genomic_DNA.
DR RefSeq; WP_004980902.1; NZ_DS999641.1.
DR AlphaFoldDB; D6A5Z2; -.
DR eggNOG; COG0045; Bacteria.
DR eggNOG; COG1042; Bacteria.
DR Proteomes; UP000003824; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR043938; Ligase_CoA_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR Pfam; PF13549; ATP-grasp_5; 1.
DR Pfam; PF13380; CoA_binding_2; 1.
DR Pfam; PF19045; Ligase_CoA_2; 1.
DR Pfam; PF13607; Succ_CoA_lig; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
PE 4: Predicted;
FT DOMAIN 258..353
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 714 AA; 75429 MW; 64C21714BEA668B1 CRC64;
MAEDRAPKVR ALLDAVRAEG RTALTAPEGK VIADAYGIAV PGEELATDVE EAVACAARFG
GSVVMKIVSP DILHKTDAGG VVVGVEGAAD VRAAFCRIVE NARAYDADAR IEGVQVQELL
PKGQEVIVGA VTDPTFGKVV AFGLGGVLVE VLKDVTFRLA PVDADEAVSM LDSIRAAEVL
RGVRGQEGVD RWAVAEQIRR VSELVTDFPE IAEVDLNPVI ATAGGAVAAD IRVILSTEQP
KERRRYSREE ILASMRRLMQ PRSVAVIGAS GEPGKIGNSV MRNLVDGGFA GEIHPVNPRT
DDILGRKAYK SVTDVPGEVD VAVFAIPARF VASALREVGR KRIPNAVLIP SGFAETGEHG
LQEEIVQVAE EYGIRLLGPN IYGYYSTWQD LCATFCTPYD VKGGVALTSQ SGGIGMAVLG
FARTTKTGVS AIVGLGNKSD LDEDDLLTWF GEDPRTECIA MHLEDLKDGR AFVEAARATV
PKKPVVVLKA GRTAAGARAA GSHTGALAGD DAVYDDILRQ AGVVRAPGLN EMLEYARALP
VLPAPQGDNV VIITGAGGSG VLLSDAVTDN GLSLMEIPPD LDAAFREFIP PFGAAGNPVD
ITGGEPPSTY EATIRLGLED PRIHALVLGY WHTIVTPPMV FAELTARVVA EFRERGISKP
VVASLAGDVE VEEACRYLFE RGVVAYPYTT EKPVAVLGAK YRWARAAGLL GGGS
//
